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    Evaluation of new chalcone derivatives as polyphenol oxidase inhibitors
    (Pergamon-Elsevier Science Ltd, 2011) Sönmez, Fatih; Sevmezler, Sedat; Atahan, Alparslan; Ceylan, Mustafa; Demir, Dudu; Gencer, Nahit; Küçükislamoğlu, Mustafa
    A newly series of 4-(phenylurenyl) chalcone (4a-j) and 4'-(phenylurenyl/thiourenyl)chalcone (9a-l) derivatives were synthesized and their inhibitory effects on the diphenolase activity of banana tyrosinase were evaluated. Tyrosinase has been purified from banana on an affinity gel comprised of Sepharose 4B-L-tyrosine-p-aminobenzoic acid. The result showed that 4a-j inhibited the PPO enzyme activity. Conversely, 9a-h and 9i-l showed activator effect on tyrosinase enzyme activity. (C) 2011 Elsevier Ltd. All rights reserved.
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    In vitro inhibition effect of some chalcones on erythrocyte carbonic anhydrase I and II
    (Taylor & Francis Ltd, 2013) Gençer, Nahit; Bilen, Çiğdem; Demir, Dudu; Atahan, Alparslan; Ceylan, Mustafa; Küçükislamoğlu, Mustafa
    In this study, 4'-(phenylurenyl/thiourenyl) chalcones (14-25) were prepared from 4'-(phenylurenyl/thiourenyl)acetophenones and benzaldehyde derivatives by Claisen-Schmidt condensation. In vitro inhibition effects of chalcone derivatives on purified carbonic anhydrase I and carbonic anhydrase II were investigated by using the CO2 hydration method of Maren. The result showed that all the synthesized compounds inhibited the CA isoenzymes activity. 18 and 19 were found to be most active (IC50 = 25.41 m M and 23.06 mu M) for hCA I, respectively. For hCA II, 24 is the most active compound (IC50 = 14.40 mu M).